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Originally published In Press as doi:10.1074/jbc.M504768200 on June 30, 2005

J. Biol. Chem., Vol. 280, Issue 35, 31003-31010, September 2, 2005
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Mechanism of Redox-mediated Guanine Nucleotide Exchange on Redox-active Rho GTPases*

Jongyun Heo{ddagger} and Sharon L. Campbell{ddagger}§

From the {ddagger}Department of Biochemistry and Biophysics, §Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599

Rho GTPases regulate multiple cellular processes including actin cytoskeletal rearrangements, transcriptional regulation, and oxidant production. The studies described herein demonstrate that small molecule redox agents, in addition to protein regulatory factors, can regulate the activity of redox-active Rho GTPases. A novel (GXXXXGK(S/T)C) motif, conserved in a number of Rho GTPases, appears critical for redox-mediated guanine nucleotide dissociation in vitro. A detailed molecular mechanism for redox regulation of GXXXXGK(S/T)C motif-containing Rho GTPases is proposed.


Received for publication, May 2, 2005 , and in revised form, June 6, 2005.

* This work was supported by National Institutes of Health Grants RO1CA89614-O1A1 and PO1 HL45100 (to S. L. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, University of North Carolina, 530 Mary Ellen Jones Bldg., Chapel Hill, NC 27599-7260. Tel.: 919-966-7139; Fax: 919-966-2852; E-mail: campbesl{at}med.unc.edu.


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